View source for 1k42


==The Solution Structure of the CBM4-2 Carbohydrate Binding Module from a Thermostable Rhodothermus marinus Xylanase.==
<StructureSection load='1k42' size='340' side='right'caption='[[1k42]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1k42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K42 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k42 OCA], [https://pdbe.org/1k42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k42 RCSB], [https://www.ebi.ac.uk/pdbsum/1k42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k42 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P96988_RHOMR P96988_RHOMR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure is presented for the second family 4 carbohydrate binding module (CBM4-2) of xylanase 10A from the thermophilic bacterium Rhodothermus marinus. CBM4-2, which binds xylan tightly, has a beta-sandwich structure formed by 11 strands, and contains a prominent cleft. From NMR titrations, it is shown that the cleft is the binding site for xylan, and that the main amino acids interacting with xylan are Asn31, Tyr69, Glu72, Phe110, Arg115, and His146. Key liganding residues are Tyr69 and Phe110, which form stacking interactions with the sugar. It is suggested that the loops on which the rings are displayed can alter their conformation on substrate binding, which may have functional importance. Comparison both with other family 4 cellulose binding modules and with the structurally similar family 22 xylan binding module shows that the key aromatic residues are in similar positions, and that the bottom of the cleft is much more hydrophobic in the cellulose binding modules than the xylan binding proteins. It is concluded that substrate specificity is determined by a combination of ring orientation and the nature of the residues lining the bottom of the binding cleft.

The solution structure of the CBM4-2 carbohydrate binding module from a thermostable Rhodothermus marinus xylanase.,Simpson PJ, Jamieson SJ, Abou-Hachem M, Karlsson EN, Gilbert HJ, Holst O, Williamson MP Biochemistry. 2002 May 7;41(18):5712-9. PMID:11980475<ref>PMID:11980475</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1k42" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodothermus marinus]]
[[Category: Abou-Hachem M]]
[[Category: Gilbert HJ]]
[[Category: Holst O]]
[[Category: Jamieson SJ]]
[[Category: Nordberg-Karlsson E]]
[[Category: Simpson PJ]]
[[Category: Williamson MP]]